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Protein

Coagulation factor X

Gene

F10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

Catalytic activityi

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei274 – 2741Charge relay systemBy similarity
Active sitei320 – 3201Charge relay systemBy similarity
Active sitei417 – 4171Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiS01.216.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor X (EC:3.4.21.6)
Alternative name(s):
Stuart factor
Cleaved into the following 3 chains:
Gene namesi
Name:F10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61850. F10.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: RGD
  • extracellular region Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: RGD
  • membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 4020By similarityPRO_0000027804Add
BLAST
Chaini41 – 482442Coagulation factor XPRO_0000027805Add
BLAST
Chaini41 – 180140Factor X light chainBy similarityPRO_0000027806Add
BLAST
Chaini184 – 482299Factor X heavy chainBy similarityPRO_0000027807Add
BLAST
Propeptidei184 – 23148Activation peptideBy similarityPRO_0000027808Add
BLAST
Chaini232 – 482251Activated factor Xa heavy chainBy similarityPRO_0000027809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi90 ↔ 101By similarity
Disulfide bondi95 ↔ 110By similarity
Modified residuei103 – 1031(3R)-3-hydroxyaspartateBy similarity
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 340Interchain (between light and heavy chains)PROSITE-ProRule annotation
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi238 ↔ 243By similarity
Disulfide bondi259 ↔ 275By similarity
Disulfide bondi388 ↔ 402By similarity
Disulfide bondi413 ↔ 441By similarity

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated.By similarity
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

PaxDbiQ63207.
PRIDEiQ63207.

PTM databases

iPTMnetiQ63207.
PhosphoSiteiQ63207.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.

Gene expression databases

BgeeiENSRNOG00000033444.
GenevisibleiQ63207. RN.

Interactioni

Subunit structurei

The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026677.

Chemistry

BindingDBiQ63207.

Structurei

3D structure databases

ProteinModelPortaliQ63207.
SMRiQ63207. Positions 42-86, 88-174, 232-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 16541EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini232 – 465234Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiQ63207.
KOiK01314.
OrthoDBiEOG091G0AH5.
PhylomeDBiQ63207.
TreeFamiTF327329.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESPVRLSLL YVVLASLLLP GRSVFINRER ANNVLQRIRR ANSFFEEIKK
60 70 80 90 100
GNLERECVEE ICSFEEAREV FEDNEKTTEF WNKYEDGDQC ESSPCQNQGE
110 120 130 140 150
CRDGLGSYTC TCTEGFEGKN CELFVRKLCS LDNGDCDQFC REEQNSVVCS
160 170 180 190 200
CAKGYFLGND GKSCLSTAPF PCGKTNKGRA KRSVALNTSN SEPDPEDLMP
210 220 230 240 250
DADILYPTES PSELLNLNKT EPEANSDDVI RIVGGQECKR GECPWQALLF
260 270 280 290 300
SDEETDGFCG GTILNEFYIL TAAHCLHQAK RFKVRVGDLN TEQEDGGEMV
310 320 330 340 350
HEVDMIIKHN KFQRDTYDFD IAMLRLKTPI TFRENVAPAC LPQKDWAEAT
360 370 380 390 400
LMTQKTGIVS GFGRTHEKGR QSKVLKMMEV PYVDRNTCRL STSFSITQNM
410 420 430 440 450
FCAGYDAKQE DACQGDSGGP HVTRFKDTYF VTGIVSWGEG CARKGKYGIY
460 470 480
TKVTAFLKWI DRSMKARVGP TSETPRLTHP PY
Length:482
Mass (Da):54,265
Last modified:November 1, 1996 - v1
Checksum:i0284678E3954A698
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79807 mRNA. Translation: CAA56202.1.
BC088151 mRNA. Translation: AAH88151.1.
PIRiS49075. EXRT.
RefSeqiNP_058839.1. NM_017143.2.
UniGeneiRn.21393.

Genome annotation databases

GeneIDi29243.
KEGGirno:29243.
UCSCiRGD:61850. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79807 mRNA. Translation: CAA56202.1.
BC088151 mRNA. Translation: AAH88151.1.
PIRiS49075. EXRT.
RefSeqiNP_058839.1. NM_017143.2.
UniGeneiRn.21393.

3D structure databases

ProteinModelPortaliQ63207.
SMRiQ63207. Positions 42-86, 88-174, 232-473.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026677.

Chemistry

BindingDBiQ63207.
ChEMBLiCHEMBL3755.

Protein family/group databases

MEROPSiS01.216.

PTM databases

iPTMnetiQ63207.
PhosphoSiteiQ63207.

Proteomic databases

PaxDbiQ63207.
PRIDEiQ63207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29243.
KEGGirno:29243.
UCSCiRGD:61850. rat.

Organism-specific databases

CTDi2159.
RGDi61850. F10.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiQ63207.
KOiK01314.
OrthoDBiEOG091G0AH5.
PhylomeDBiQ63207.
TreeFamiTF327329.

Miscellaneous databases

PROiQ63207.

Gene expression databases

BgeeiENSRNOG00000033444.
GenevisibleiQ63207. RN.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA10_RAT
AccessioniPrimary (citable) accession number: Q63207
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.